Abstract
It is stressed that the presence of a metal ion directly bound to a protein can introduce elements of complexity, such as vibronic coupling, which cannot be ruled outa priori. As a typical example, two copper proteins, azurin and plastocyanin, have been considered. Electron paramagnetic resonance spectra of the two proteins, recorded in the range 4–200 K and with different cooling rates, support the hypothesis of a prominent role played by vibronic interactions as well as by the conformational substate distribution.
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Bacci, M., Cannistraro, S. Role of vibronic coupling and of conformational substate distribution in determining the features of copper-protein EPR spectra. Appl Magn Reson 1, 369–378 (1990). https://doi.org/10.1007/BF03166020
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DOI: https://doi.org/10.1007/BF03166020